ArticleFrontiers in immunology2022
Duck gasdermin E is a substrate of caspase-3/-7 and an executioner of pyroptosis.
Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Infectious bursal disease virus induces GSDME-dependent pyroptosis via the mitochondrial caspase-9/3 pathway in DF-1 cells.Veterinary research · 2026Article
- Novel duck reovirus σC hijacks the mitochondrial COQ6-CoQ10 axis to drive NLRP3-dependent pyroptosis.PLoS pathogens · 2026Article
- Chicken GSDME, a major pore-forming molecule responsible for RNA virus-induced pyroptosis in chicken.Journal of virology · 2025Article
- Caspase-1 activates gasdermin A in non-mammals.eLife · 2024Article
- Molecular mechanisms of gasdermin D pore-forming activity.Nature immunology · 2023Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gasdermin (GSDM)-mediated cell death is an ancient immune defensive mechanism that plays an essential role in bacteria, fungi, coral, teleost, and mammals. After being cleaved by proteases of hosts or pathogens, amino-terminal (NT) fragment of GSDMs (GSDM-NTs) form pores in the membrane structure of cells, thereby leading to pyroptotic cell death. However, the expression profile, activation mechanism and function of avian GSDMs have not been studied in depth yet. In the current study, genes encoding duck gasdermin E (duGSDME), caspase-3 (ducaspase-3) and ducaspase-7 were cloned from mRNA of a virus-challenged duck embryo. The cleavage of duGSDME by ducaspase-3/-7 was verified in the cell-free system and/or in human embryonic kidney cells (HEK293). Ducaspase-3/-7 could recognize and cleave duGSDME at 270DAVD273. Overexpression of duGSDME-NT (1-273aa) fragment led to pyroptosis-like morphological change, increased lactic dehydrogenase (LDH) release and propidium iodide uptake of HEK293 cells, which indicated that duGSDME-NTs could cause cell membrane damage. In addition, recombinantly expressed duGSDME-NT showed bactericidal activity to an enterotoxic
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